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表面蛋白抗原Ⅰ/Ⅱ(AgⅠ/Ⅱ、P1、PAc、SpaP、SspA、SspB等)广泛存在于口腔链球菌细胞壁表面,介导变异链球菌、表兄链球菌、格登链球菌等口腔链球菌与牙表面的黏附,影响牙菌斑的形成,是影响龋病形成和发展的主要毒力因子之一。自有研究报道了变异链球菌表面蛋白抗原Ⅰ/Ⅱ的V区(SpaP-V)晶体结构之后,陆续有其AgⅠ/Ⅱ的三维结构、格登链球菌V区(SspB-V)的三维结构和C末端(SspB-C)的三维结构见诸报道,逐步揭示了口腔链球菌表面蛋白抗原Ⅰ/Ⅱ的三维立体结构,进一步解释了其功能机制。本文就口腔链球菌表面蛋白抗原的三维结构和相关功能表位的研究情况作一综述。
Surface protein antigens Ⅰ / Ⅱ (AgⅠ / Ⅱ, P1, PAc, SpaP, SspA, SspB, etc.) are widely present on the cell wall surface of Streptococcus oralis and mediate Streptococcus mutans, Streptococcus sobrinus and Streptococcus Tooth surface adhesion, affecting the formation of plaque, dental caries affect the formation and development of one of the major virulence factors. After the self-reported crystal structure of SpaP-V of Streptococcus mutans surface protein antigen Ⅰ / Ⅱ, the three-dimensional structure of AgⅠ / Ⅱ and the three-dimensional structure of Streptococcus granulosus V region (SspB-V) The three-dimensional structure of the C-terminal (SspB-C) has been reported, revealing the three-dimensional structure of oral buccal surface antigen Ⅰ / Ⅱ, and further explaining its functional mechanism. This article reviews the three-dimensional structure of Streptococcus oralis surface protein antigen and related functional epitopes.